Evidence map›Paper›PMID 24002823›Full record

ArticleAAPS PharmSciTech2013

Orthogonal high-throughput thermal scanning method for rank ordering protein formulations.

Vishal C Nashine, Andrew M Kroetsch, Erinc Sahin, Rong Zhou, Monica L Adams

Open access · bronzeAbstract read
In one paragraph

Article in AAPS PharmSciTech, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 26% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. The dye SYPRO orange binds to amylin amyloid fibrils but not pre-fibrillar intermediates.Protein science : a publication of the Protein Society · 2016
    Article
  4. Article
  5. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Vishal C NashineDrug Product Science and Technology, Bristol-Myers Squibb, 1 Squibb Drive, New Brunswick, New Jersey, 08903, USA, vishal.nashine@bms.com.
Andrew M Kroetsch
Erinc Sahin
Rong Zhou
Monica L Adams
Bristol-Myers Squibb (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A high-throughput thermal-scanning method to rank-order formulation conditions for therapeutic proteins is described. Apparent transition temperatures for unfolding and aggregation of four different proteins are determined using the dyes SYPRO Orange and thioflavin T (ThT) under a variety of buffer conditions. The results indicate that the ThT-based thermal scanning method offers several advantages over the previously described SYPRO Orange-based thermal scanning and allows rapid rank ordering of solution conditions relevant toward long-term storage of therapeutic molecules. The method is also amenable to high protein concentration and does not require sample dilution or extensive preparation. Additionally, this parallel use of SYPRO Orange and ThT can be readily applied to the screening of mutants for their unfolding and aggregation propensities.

Indexed as

AlgorithmsAntibodies, MonoclonalBenzothiazolesBuffersChemistry, PharmaceuticalChymotrypsinogenHigh-Throughput Screening AssaysPeptidesProtein ConformationProteinsProtein Structure, SecondaryReal-Time Polymerase Chain ReactionSolubilitySpectrometry, FluorescenceTemperatureThiazolesAntibodies, MonoclonalBenzothiazolesBuffersChymotrypsinogenPeptidesProteinsThiazolesthioflavin T

Identifiers

PMID24002823
PMCPMC3840783
OpenAlexW2067308668

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.